ID A0A365NZN7_9FLAO Unreviewed; 357 AA.
AC A0A365NZN7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093,
GN ECO:0000313|EMBL:RBA27584.1};
GN ORFNames=DPN68_11450 {ECO:0000313|EMBL:RBA27584.1};
OS Flavobacterium tibetense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2233533 {ECO:0000313|EMBL:RBA27584.1, ECO:0000313|Proteomes:UP000253319};
RN [1] {ECO:0000313|EMBL:RBA27584.1, ECO:0000313|Proteomes:UP000253319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH5 {ECO:0000313|EMBL:RBA27584.1,
RC ECO:0000313|Proteomes:UP000253319};
RA Xing P., Phurbu D., Lu H.;
RT "Flavobacterium tibetense sp. nov., isolated from a wetland YonghuCo on
RT Tibetan Plateau.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA. {ECO:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBA27584.1}.
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DR EMBL; QLST01000016; RBA27584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365NZN7; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000253319; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
DR HAMAP; MF_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Reference proteome {ECO:0000313|Proteomes:UP000253319}.
FT DOMAIN 63..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40484 MW; E034057EBEE3D2F2 CRC64;
MLDRLQYVKQ RFDEISDLII QPDVIADQKR YVQLNKEYKD LKGLVEKREE YIVLDGNIKE
AQEIIADGSD AEMVEMAKMQ LEEAKERLPQ LEEEIKFMLI PKDPEDAKNV MVEIRAGTGG
DEASIFAGDL FRMYTKYCEA RGWRTSVVDV SEGTSGGFKE IIFEVTGEDV YGTLKFEAGV
HRVQRVPQTE TQGRVHTSAA TVMVLPEAEE FDVQIDMNDV RVDFFCSSGP GGQSVNTTKS
AVRLTHIPTG LVAQCQDQKS QHKNKDKALE VLRSRLYEKE LAIKQAEDAT KRSSQVSSGD
RSAKIRTYNY SQGRVTDHRI GLDVFDMDGV MNGKIQKFVD ELQMVNNMEK LKENEVF
//